ID S7MU98_MYOBR Unreviewed; 309 AA.
AC S7MU98;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
GN ORFNames=D623_10015592 {ECO:0000313|EMBL:EPQ08061.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08061.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- FUNCTION: Thin filament-associated protein that is implicated in the
CC regulation and modulation of smooth muscle contraction. It is capable
CC of binding to actin, calmodulin and tropomyosin. The interaction of
CC calponin with actin inhibits the actomyosin Mg-ATPase activity.
CC {ECO:0000256|ARBA:ARBA00025109, ECO:0000256|RuleBase:RU361224}.
CC -!- SIMILARITY: Belongs to the calponin family.
CC {ECO:0000256|ARBA:ARBA00009631, ECO:0000256|RuleBase:RU361224}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE162397; EPQ08061.1; -; Genomic_DNA.
DR RefSeq; XP_005866734.1; XM_005866672.1.
DR AlphaFoldDB; S7MU98; -.
DR GeneID; 102263212; -.
DR KEGG; myb:102263212; -.
DR CTD; 1265; -.
DR eggNOG; KOG2046; Eukaryota.
DR OrthoDB; 11630at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR CDD; cd21283; CH_CNN2; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR001997; Calponin/LIMCH1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR PANTHER; PTHR47385; CALPONIN; 1.
DR PANTHER; PTHR47385:SF7; CALPONIN-2; 1.
DR Pfam; PF00402; Calponin; 3.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00889; CALPONIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR PROSITE; PS01052; CALPONIN_1; 2.
DR PROSITE; PS51122; CALPONIN_2; 3.
DR PROSITE; PS50021; CH; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|RuleBase:RU361224};
KW Calmodulin-binding {ECO:0000256|RuleBase:RU361224};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 28..132
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 280..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 33679 MW; CE2EE8CA91AE7DC4 CRC64;
MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRGWIEG LTGLSIGPDF QKGLKDGIIL
CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV
QVSLLALAGK AKTKGLQSGV DIGIKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG
MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC
DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGQMA DGAPGSVGDC PSPGKAPEYP
PYYQEEAGY
//
